Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
about
Folding of hepatitis C virus E1 glycoprotein in a cell-free system.Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatinA transcriptome-proteome integrated network identifies endoplasmic reticulum thiol oxidoreductase (ERp57) as a hub that mediates bone metastasisThe oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I moleculesChanges in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamineComparative Analysis of the Interaction between Different Flavonoids and PDIA3Nck-dependent activation of extracellular signal-regulated kinase-1 and regulation of cell survival during endoplasmic reticulum stress.Study of therapy resistance in cancer cells with functional proteome analysis.Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.Glycoprotein folding in the endoplasmic reticulum.Glycohistochemistry: the why and how of detection and localization of endogenous lectins.The signal sequence influences post-translational ER translocation at distinct stages.Dealing with misfolded proteins: examining the neuroprotective role of molecular chaperones in neurodegeneration.Role of calnexin in the glycan-independent quality control of proteolipid protein.Construction of a high-mannose-type glycan library by a renewed top-down chemo-enzymatic approach.Intracellular trafficking of P-glycoprotein.Polytopic membrane protein folding and assembly in vitro and in vivo.Approaches toward High-Mannose-Type Glycan Libraries.Selective loss of RPGRIP1-dependent ciliary targeting of NPHP4, RPGR and SDCCAG8 underlies the degeneration of photoreceptor neuronsCa2+-dependent redox modulation of SERCA 2b by ERp57.Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness.The atrazine metabolite diaminochlorotriazine suppresses LH release from murine LβT2 cells by suppressing GnRH-induced intracellular calcium transients.Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.N-linked oligosaccharide chains of Sendai virus fusion protein determine the interaction with endoplasmic reticulum molecular chaperones.Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates.The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo.Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein.The primary substrate binding site in the b' domain of ERp57 is adapted for endoplasmic reticulum lectin association.Maturation of hepatic lipase. Formation of functional enzyme in the endoplasmic reticulum is the rate-limiting step in its secretion.Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function.Extracellular Thiol Isomerases and Their Role in Thrombus FormationCFTR and Ca Signaling in Cystic Fibrosis.Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis.Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein.High-level expression and purification of Cys-loop ligand-gated ion channels in a tetracycline-inducible stable mammalian cell line: GABAA and serotonin receptorsApical transport and folding of prostate-specific membrane antigen occurs independent of glycan processing.The use of calnexin and calreticulin by cellular and viral glycoproteins.Identification and characterization of structural domains of human ERp57: association with calreticulin requires several domains.The prosequence of human lactase-phlorizin hydrolase modulates the folding of the mature enzyme.The CCAAT box in the proximal SERCA2 gene promoter regulates basal and stress-induced transcription in cardiomyocytes.
P2860
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P2860
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
description
2000 nî lūn-bûn
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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
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2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年學術文章
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name
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
@ast
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
@en
type
label
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
@ast
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
@en
prefLabel
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
@ast
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
@en
P2093
P1433
P1476
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?
@en
P2093
F J Lecomte
J D Oliver
S J Russell
P356
10.1016/S0014-5793(00)01666-5
P407
P577
2000-06-01T00:00:00Z